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Results for
""Proton-Translocating ATPases""[mesh_terms]

301 Results

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The physiological role of complex V in ATP synthesis: Murzyme functioning is viable whereas rotary conformation change model is untenable.

Kelath Murali Manoj, Nikolai Mikhailovich Bazhin, Hirohisa Tamagawa, Laurent Jaeken, Abhinav Parashar

Journal of biomolecular structure & dynamics 2023;41(9):3993-4012

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Rotary Ion-Translocating ATPases/ATP Synthases: Diversity, Similarities, and Differences.

T E Shugaeva, A V Litvin, B A Feniouk, A S Lapashina, V M Zubareva

Biochemistry. Biokhimiia 2021;85(12):1613-1630

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Regulatory mechanisms of proton-translocating F(O)F (1)-ATP synthase.

Masasuke Yoshida, Boris A Feniouk

Results and problems in cell differentiation 2008;45():279-308

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Composition and assembly of the yeast vacuolar H(+)-ATPase complex.

L A Graham, B Powell, T H Stevens

The Journal of experimental biology 2000;203(Pt 1):61-70

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Transport ATPases in biological systems and relationship to human disease: a brief overview.

Peter L Pedersen

Journal of bioenergetics and biomembranes 2003;34(5):327-32

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Proton translocation driven by ATP hydrolysis in V-ATPases.

Shoko Kawasaki-Nishi, Tsuyoshi Nishi, Michael Forgac

FEBS letters 2003;545(1):76-85

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ATP synthase in mycobacteria: special features and implications for a function as drug target.

Ping Lu, Holger Lill, Dirk Bald

Biochimica et biophysica acta 2014;1837(7):1208-18

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The rotary mechanism of ATP synthase.

D Stock, C Gibbons, I Arechaga, A G Leslie, J E Walker

Current opinion in structural biology 2001;10(6):672-9

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Structure and function of subunit a of the ATP synthase of Escherichia coli.

Steven B Vik, Robert R Ishmukhametov

Journal of bioenergetics and biomembranes 2006;37(6):445-9

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What Are the Implications of Cr(III) Serving as an Inhibitor of the Beta Subunit of Mitochondrial ATP Synthase?

John B Vincent

Biological trace element research 2024;202(4):1335-1344

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AtpΘ is an inhibitor of FF ATP synthase to arrest ATP hydrolysis during low-energy conditions in cyanobacteria.

Kuo Song, Desirée Baumgartner, Martin Hagemann, Alicia M Muro-Pastor, Sandra Maaß, Dörte Becher, Wolfgang R Hess

Current biology : CB 2022;32(1):136-148.e5

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Catalytic properties of Na(+)-translocating V-ATPase in Enterococcus hirae.

T Murata, M Kawano, K Igarashi, I Yamato, Y Kakinuma

Biochimica et biophysica acta 2001;1505(1):75-81

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Zooming in on ATP hydrolysis in F1.

Klaus Schulten, Markus Dittrich

Journal of bioenergetics and biomembranes 2006;37(6):441-4

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Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps.

Katarzyna Kabała, Małgorzata Janicka

International journal of molecular sciences 2023;24(5):4512

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Structural and functional features of the Escherichia coli F1-ATPase.

G Gruber

Journal of bioenergetics and biomembranes 2002;32(4):341-6

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Results: 1 – 15 / 301

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Results for ""Proton-Translocating ATPases""[mesh_terms]

The physiological role of complex V in ATP synthesis: Murzyme functioning is viable whereas rotary conformation change model is untenable.

Rotary Ion-Translocating ATPases/ATP Synthases: Diversity, Similarities, and Differences.

Regulatory mechanisms of proton-translocating F(O)F (1)-ATP synthase.

Composition and assembly of the yeast vacuolar H(+)-ATPase complex.

Transport ATPases in biological systems and relationship to human disease: a brief overview.

Proton translocation driven by ATP hydrolysis in V-ATPases.

ATP synthase in mycobacteria: special features and implications for a function as drug target.

The rotary mechanism of ATP synthase.

Structure and function of subunit a of the ATP synthase of Escherichia coli.

What Are the Implications of Cr(III) Serving as an Inhibitor of the Beta Subunit of Mitochondrial ATP Synthase?

AtpΘ is an inhibitor of FF ATP synthase to arrest ATP hydrolysis during low-energy conditions in cyanobacteria.

Catalytic properties of Na(+)-translocating V-ATPase in Enterococcus hirae.

Zooming in on ATP hydrolysis in F1.

Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps.

Structural and functional features of the Escherichia coli F1-ATPase.

Results for
""Proton-Translocating ATPases""[mesh_terms]